Inhibition of membrane fusion proteins
a technology of membrane fusion and protein, which is applied in the field of viral infection control, can solve the problems of insufficient antiviral strategies and sorely needed alternative strategies, and achieve the effects of inhibiting infection, and reducing quenching of fluorescent molecules
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Domain III from Class III Fusion Proteins Functions as a Dominant-Negative Inhibitor of Virus Membrane Fusion
[0186]Rationale and domain III expression. The structure of the class II homotrimer suggests several features that might be targets for inhibition of the fusion reaction. The pH 7 form of the dengue virus E protein crystallized with a molecule of detergent bound in a hydrophobic pocket near the “hinge” region between domains 1 and II (Modis et al., 2003). As the hinge changes its angle during the transition to the trimer form, inhibition of this flexibility may block fusion and infection. Thus, molecules that dock into the hydrophobic pocket are potential antivirals (Modis et al., 2003). The structure of the fusion protein homotrimer reveals that the “stem” region of the protein interacts (or would be predicted to interact in the case of the dengue HT and TBE HT, which do not contain the stem) with an HT core region composed of domains I and II (see stem in FIG. 3 schematic)....
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